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Literature summary for 2.4.1.227 extracted from
- Enzyme function is regulated by its localization (2015), Comput. Biol. Chem., 59 Pt B, 113-122.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene murG, expression of C-terminal YFP-tagged enzyme in a murG-deficient strain of Bacillus subtilis | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F77E | site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type. Lipid II synthesis might be totally abrogated in mutant F77E explaining why the mutant is blocked in septation, cell wall synthesis is necessary for engulfment | Bacillus subtilis |
| additional information | none of the point mutations shows lethality and cells expressing MurG-GFP point mutants grow normally in absence of the wild-type murG allele | Bacillus subtilis |
| S67E | site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type | Bacillus subtilis |
| V74E | site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type. Lipid II synthesis might be totally abrogated in mutant V74E explaining why the mutant is blocked in septation, cell wall synthesis is necessary for engulfment | Bacillus subtilis |
| V81E | site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type | Bacillus subtilis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell septum | during exponential growth, MurG localizes to septa of Bacillus subtilis, a zone of active peptidoglycan synthesis, and its N-terminal amphipathic helix is dispensable | Bacillus subtilis | 30428 | - |
| forespore | - |
Bacillus subtilis | - |
- |
| membrane | the enzyme localization to the membrane depends on the phospholipid cardiolipin | Bacillus subtilis | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MurG | - |
Bacillus subtilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | point mutations in a MurG helical causes severe sporulation defects, but does not affect localization nor cause detectable defects during exponential growth. In strains in which the cardiolipin-synthesizing genes are deleted, MurG levels are diminished at the forespore, but MurG localization during sporulation is rescued by external addition of purified cardiolipin. During sporulation, lack of MurG localization heavily affects engulfment dynamics and sporulation efficiency, indicating a defect in MurG enzymatic activity linked to its diffuse localization | Bacillus subtilis |
| physiological function | the glycosyltransferase MurG is necessary for cell wall synthesis at the spore during sporulation in the bacterium Bacillus subtilis. The enzyme localization is a critical factor in the regulation of proper enzyme function and catalysis | Bacillus subtilis |
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